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Protein Page:
Calnexin (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Calnexin a calcium-binding protein of the calreticulin family. A type I membrane protein of the endoplasmic reticulum .Interacts with newly synthesized glycoproteins in the endoplasmic reticulum. May act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Endoplasmic reticulum; Calcium-binding protein; Motility/polarity/chemotaxis
Cellular Component: dendrite cytoplasm; endoplasmic reticulum membrane; protein complex; cell soma; endoplasmic reticulum lumen; axon; endoplasmic reticulum; dendritic spine; melanosome; ribosome
Molecular Function: ionotropic glutamate receptor binding; protein binding; unfolded protein binding; apolipoprotein binding; calcium ion binding; glycoprotein binding
Biological Process: antigen processing and presentation of peptide antigen via MHC class I; cellular protein metabolic process; protein folding; synaptic vesicle endocytosis; protein secretion; antigen processing and presentation of exogenous peptide antigen via MHC class II; protein amino acid N-linked glycosylation via asparagine; post-translational protein modification; aging
Reference #:  P27824 (UniProtKB)
Alt. Names/Synonyms: Calnexin; CALX; CANX; CNX; FLJ26570; IP90; Major histocompatibility complex class I antigen-binding protein p88; p90
Gene Symbols: CANX
Molecular weight: 67,568 Da
Basal Isoelectric point: 4.47  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Calnexin

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S55 DTTAPPSSPKVtYKA
0 1 T59-ga PPSSPKVtYKAPVPt
0 1 T66-ga tYKAPVPtGEVyFAD
0 6 Y70-p PVPtGEVyFADSFDR
0 1 T79-ga ADSFDRGtLsGWILS
0 1 S81-p SFDRGtLsGWILSKA
0 1 K103-u EIAKYDGkWEVEEMK
0 1 K118-u ESKLPGDkGLVLMSR
0 1 S132 RAKHHAISAKLNkPF
0 2 K137-a AISAKLNkPFLFDTK
0 1 K137-u AISAKLNkPFLFDTK
0 2 K170-u AYVKLLSkTPELNLD
0 1 K182-u NLDQFHDkTPYTIMF
0 1 Y185 QFHDkTPYTIMFGPD
0 1 T186 FHDkTPYTIMFGPDK
0 33 Y214-p KNPKTGIyEEKHAKR
0 1 K217 KTGIyEEKHAKRPDA
0 2 K227-u KRPDADLkTYFTDKK
0 28 Y379-p PVIDNPNyKGKWKPP
0 2 K398-u PSYQGIWkPRkIPNP
0 2 K401-u QGIWkPRkIPNPDFF
0 28 K458-a ANDGWGLkkAADGAA
0 1 K458-u ANDGWGLkkAADGAA
0 3 K459-a NDGWGLkkAADGAAE
0 3 K459-u NDGWGLkkAADGAAE
0 3 K516-u TSGMEYKkTDAPQPD
0 3 K525-u DAPQPDVkEEEEEKE
0 1 K535 EEEKEEEKDkGDEEE
0 2 K537-u EKEEEKDkGDEEEEG
0 3 K547-u EEEEGEEkLEEKQKs
0 2 K551 GEEkLEEKQKsDAEE
2 111 S554-p kLEEKQKsDAEEDGG
0 35 T562-p DAEEDGGtVsQEEED
5 88 S564-p EEDGGtVsQEEEDRK
0 6 R570 VsQEEEDRKPKAEED
4 132 S583-p EDEILNRsPRNRKPR
  mouse

 
S56-p SDASTPPsPKVTYKA
T60 TPPsPKVTYKAPVPT
T67 TYKAPVPTGEVYFAD
Y71 PVPTGEVYFADSFDR
S80 ADSFDRGSLsGWILS
S82-p SFDRGSLsGWILSKA
K104 EIAKYDGKWEVDEMK
K119 ETKLPGDKGLVLMSR
S133-p RAKHHAIsAKLNKPF
K138 AIsAKLNKPFLFDTK
K138 AIsAKLNKPFLFDTK
K171-u AYVKLLSkTAELSLD
K183 SLDQFHDKTPytIMF
Y186-p QFHDKTPytIMFGPD
T187-p FHDKTPytIMFGPDK
Y215 KNPKTGVYEEkHAKR
K218-a KTGVYEEkHAKRPDA
K228 KRPDADLKTYFTDKK
Y380 PMIDNPNYKGKWKPP
K399 PNYQGIWKPRKIPNP
K402 QGIWKPRKIPNPDFF
K459-a ANDGWGLkkAADGAA
K459 ANDGWGLKkAADGAA
K460-a NDGWGLkkAADGAAE
K460 NDGWGLkKAADGAAE
K517-u SNAMEYKkTDAPQPD
K526-u DAPQPDVkDEEGKEE
K535-u EEGKEEEkNkRDEEE
K537-u GKEEEkNkRDEEEEE
K546-u DEEEEEEkLEEkQKs
K550-u EEEkLEEkQKsDAEE
S553-p kLEEkQKsDAEEDGV
T561-p DAEEDGVtGsQDEED
S563-p EEDGVtGsQDEEDsK
S569-p GsQDEEDsKPKAEED
S582-p EDEILNRsPRNRKPR
  rat

 
S56 SDTSTPPSPKVTYKA
T60 TPPSPKVTYKAPVPT
T67 TYKAPVPTGEVYFAD
Y71 PVPTGEVYFADSFDR
S80 ADSFDRGSLSGWILS
S82 SFDRGSLSGWILSKA
K104 EIAKYDGKWEVDEMK
K119 ETKLPGDKGLVLMSR
S133 RAKHHAISAKLNKPF
K138 AISAKLNKPFLFDTK
K138 AISAKLNKPFLFDTK
K171 AYVKLLSKTSELNLD
K183 NLDQFHDKTPYTIMF
Y186 QFHDKTPYTIMFGPD
T187 FHDKTPYTIMFGPDK
Y215 KNPKTGVYEEKHAKR
K218 KTGVYEEKHAKRPDA
K228 KRPDADLKTYFTDKK
Y380 PMIDNPNYKGKWKPP
K399 PNYQGIWKPRKIPNP
K402 QGIWKPRKIPNPDFF
K459-a ANDGWGLkKAADGAA
K459 ANDGWGLKKAADGAA
K460 NDGWGLkKAADGAAE
K460 NDGWGLkKAADGAAE
K517 SNAMEYKKTDAPQPD
K526 DAPQPDVKDEEGKEE
K535 EEGKEEEKNKGDEEE
K537 GKEEEKNKGDEEEEE
K546 DEEEEEEKLEEKQKs
K550 EEEKLEEKQKsDAEE
S553-p KLEEKQKsDAEEDGG
T561-p DAEEDGGtGsQDEED
S563-p EEDGGtGsQDEEDSK
S569 GsQDEEDSKPKAEED
S582-p EDEILNRsPRNRKPR
  dog

 
S56 PDTSAPTSPKVTYKA
T60 APTSPKVTYKAPVPT
T67 TYKAPVPTGEVYFAD
Y71 PVPTGEVYFADSFDR
T80 ADSFDRGTLSGWILS
S82 SFDRGTLSGWILSKA
K104 EIAKYDGKWEVDEMK
K119 ETKLPGDKGLVLMSR
S133 RAKHHAISAKLNKPF
K138 AISAKLNKPFLFDTK
K138 AISAKLNKPFLFDTK
K171 AYVKLLSKTPELNLD
K183 NLDQFHDKTPYTIMF
Y186 QFHDKTPYTIMFGPD
T187 FHDKTPYTIMFGPDK
Y215 KNPKTGVYEEKHAKR
K218 KTGVYEEKHAKRPDA
K228 KRPDADLKTYFTDKK
Y380 PMIDNPNYKGKWKPP
K399 PNYQGIWKPRKIPNP
K402 QGIWKPRKIPNPDFF
K459 ANDGWGLKKAADGAA
K459 ANDGWGLKKAADGAA
K460 NDGWGLKKAADGAAE
K460 NDGWGLKKAADGAAE
K517 SSPVEYKKTDAPQPD
K526 DAPQPDVKEEEEEKE
K536 EEEKEEEKDKGDEEE
K538 EKEEEKDKGDEEEEG
K548 EEEEGEEKLEEKQKs
K552 GEEKLEEKQKsDAEE
S555-p KLEEKQKsDAEEDGG
T563 DAEEDGGTAsQEEDD
S565-p EEDGGTAsQEEDDRK
R571 AsQEEDDRKPKAEED
S584 EDEILNRSPRNRKPR
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